Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes.
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes.
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes.
J Inorg Biochem. 2010 Oct;104(10):1063-70
Authors: Du Z, Unno M, Matsui T, Ikeda-Saito M, La Mar GN
Proton 2D NMR was used to confirm in solution a highly conserved portion of the molecular structure upon substrate loss for the...
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02-10-2011 03:51 PM
Site-specific free energy changes in proteins upon ligand binding by NMR: Ca(2+) -displacement by Ln(3+) in a Ca(2+) -binding protein from Entamoeba histolytica.
Site-specific free energy changes in proteins upon ligand binding by NMR: Ca(2+) -displacement by Ln(3+) in a Ca(2+) -binding protein from Entamoeba histolytica.
Site-specific free energy changes in proteins upon ligand binding by NMR: Ca(2+) -displacement by Ln(3+) in a Ca(2+) -binding protein from Entamoeba histolytica.
Chem Biol Drug Des. 2011 Jan 14;
Authors: Chandra K, Mustafi SM, Muthukumar S, Chary KV
The study of protein-ligand interaction has been of a great interest in contemporary structural biology. The understanding of the nature...
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01-18-2011 10:22 PM
[NMR paper] Cell-free synthesis of 15N-labeled proteins for NMR studies.
Cell-free synthesis of 15N-labeled proteins for NMR studies.
Related Articles Cell-free synthesis of 15N-labeled proteins for NMR studies.
IUBMB Life. 2005 Sep;57(9):615-22
Authors: Ozawa K, Dixon NE, Otting G
Modern cell-free in vitro protein synthesis systems present powerful tools for the synthesis of isotope-labeled proteins in high yields. The production of selectively 15 N-labeled proteins from 15 N-labeled amino acids is particularly economic and yields are often sufficient to analyze the proteins very quickly by two-dimensional NMR...
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12-01-2010 06:56 PM
[NMR paper] Preparation, characterization, and NMR spectroscopy of encapsulated proteins dissolve
Preparation, characterization, and NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids.
Related Articles Preparation, characterization, and NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids.
J Biomol NMR. 2003 Apr;25(4):313-23
Authors: Babu CR, Flynn PF, Wand AJ
Encapsulating a protein in a reverse micelle and dissolving it in a low-viscosity solvent can lower the rotational correlation time of a protein and thereby provides a novel strategy for studying proteins in a variety of contexts. The...
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11-24-2010 09:01 PM
[NMR paper] Free-energy calculations highlight differences in accuracy between X-ray and NMR stru
Free-energy calculations highlight differences in accuracy between X-ray and NMR structures and add value to protein structure prediction.
Related Articles Free-energy calculations highlight differences in accuracy between X-ray and NMR structures and add value to protein structure prediction.
Structure. 2001 Oct;9(10):905-16
Authors: Lee MR, Kollman PA
BACKGROUND: While X-ray crystallography structures of proteins are considerably more reliable than those from NMR spectroscopy, it has been difficult to assess the inherent accuracy of NMR...
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11-19-2010 08:44 PM
[NMR paper] The pressure-temperature free energy-landscape of staphylococcal nuclease monitored b
The pressure-temperature free energy-landscape of staphylococcal nuclease monitored by (1)H NMR.
Related Articles The pressure-temperature free energy-landscape of staphylococcal nuclease monitored by (1)H NMR.
J Mol Biol. 2000 Apr 28;298(2):293-302
Authors: Lassalle MW, Yamada H, Akasaka K
The thermodynamic stability of staphylococcal nuclease was studied against the variation of both temperature and pressure by utilizing (1)H NMR spectroscopy at 750 MHz in 20 mM Mes buffer containing 99.9 % (2)H(2)O, pH 5.3. Equilibrium fractions of folded...
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11-18-2010 09:15 PM
Characterization of caged compounds binding to proteins by NMR spectroscopy.
Characterization of caged compounds binding to proteins by NMR spectroscopy.
Characterization of caged compounds binding to proteins by NMR spectroscopy.
Biochem Biophys Res Commun. 2010 Aug 27;
Authors: Bandorowicz-Pikula J, Buchet R, Cañada FJ, Clémancey M, Groves P, Jiménez-Barbero J, Lancelin JM, Marcillat O, Pikula S, Sekrecka-Belniak A, Strzelecka-Kiliszek A
Photolysable caged ligands are used to investigate protein function and activity. Here, we investigate the binding properties of caged nucleotides and their photo released...
Characterization of Free Energy Landscapes of Proteins using NMR Spectroscopy
Linear Mode
